Structure of the host-recognition device of Staphylococcus aureus phage ϕ11

被引：0

作者：

Cengiz Koç

Guoqing Xia

Petra Kühner

Silvia Spinelli

Alain Roussel

Christian Cambillau

Thilo Stehle

机构：

[1] Interfaculty Institute of Biochemistry,Department of Pediatrics

[2] University of Tübingen,undefined

[3] Interfaculty Institute of Microbiology and Infection Medicine,undefined

[4] University of Tübingen,undefined

[5] German Center for Infection Research (DZIF),undefined

[6] partner site Tübingen,undefined

[7] Institute of Inflammation and Repair,undefined

[8] Faculty of Medical and Human Sciences,undefined

[9] University of Manchester,undefined

[10] Architecture et Fonction des Macromolécules Biologiques,undefined

[11] Aix-Marseille Université,undefined

[12] Architecture et Fonction des Macromolécules Biologiques,undefined

[13] Centre National de la Recherche Scientifique,undefined

[14] Vanderbilt University School of Medicine,undefined

来源：

Scientific Reports | / 6卷

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摘要：

Phages play key roles in the pathogenicity and adaptation of the human pathogen Staphylococcus aureus. However, little is known about the molecular recognition events that mediate phage adsorption to the surface of S. aureus. The lysogenic siphophage ϕ11 infects S. aureus SA113. It was shown previously that ϕ11 requires α- or β-N-acetylglucosamine (GlcNAc) moieties on cell wall teichoic acid (WTA) for adsorption. Gp45 was identified as the receptor binding protein (RBP) involved in this process and GlcNAc residues on WTA were found to be the key component of the ϕ11 receptor. Here we report the crystal structure of the RBP of ϕ11, which assembles into a large, multidomain homotrimer. Each monomer contains a five-bladed propeller domain with a cavity that could accommodate a GlcNAc moiety. An electron microscopy reconstruction of the ϕ11 host adhesion component, the baseplate, reveals that six RBP trimers are assembled around the baseplate core. The Gp45 and baseplate structures provide insights into the overall organization and molecular recognition process of the phage ϕ11 tail. This assembly is conserved among most glycan-recognizing Siphoviridae, and the RBP orientation would allow host adhesion and infection without an activation step.

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